Modify the structure to show the amino acid hydrolysis products of this digestion, including the appropriate protonation and charge for each carboxyl and amino group at pH 7. Use the erase tool to remove bonds where necessary.
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Modify the structure to show the amino acid hydrolysis products of this digestion, including the appropriate protonation and charge for each carboxyl and amino group at pH 7. Use the erase tool to remove bonds where necessary.
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- the pKa values for phenylalanine are 1.83 (carboxyl group) and 9.13 (amino group). Use the Henderson-hasselbach equation to determine the ratio of the acidic and basic forms of each of the ionizing groups of phenylalanine at neutral pH. Based on this, draw the predominant structure of phenylalanine at neutral pH.CHOICES: Physical Agent 2. Base Analogs 3. Alkylating Agent 4. Intercalating Agent 5. Metal ions 6. Biological Agent Similar to the bases of DNA or chemicals that have a structural resemblance to the DNA bases 123456 Disrupt DNA structures and can cause frameshift mutation 123456 Denatures DNA and causes breakage or cleavage of the phosphodiester bonds through heat 123456 Induces the base-pairing errors that increases the ionization and production of gaps in the strand of the DNA. 123456 Producing ROS (reactive oxygen species), hindering the DNA repair pathway. 123456 Non-coding DNA sequences, jumps from one place to another place in a genome and influence the function of genes. 123456 Ethylnitrosourea 123456 Causes cross-linking and generation of nucleotide dimers. 123456 Able to hotwire our DNA make up and cause disease by expressing genes that causes abnormal production…Modify isoleucine to show its structure at pH 1 and pH 13. Modify each amino acid by adding or removing atoms or bonds and by adding charges where appropriate. pH 1 pH 13 Select Draw Rings More Erase Rings More Erase C с CH₂ CH₂ H₂C H₂N 1 CH₂ | CH | 310 H― H O H N U с || 0 H Q2 Q Select Draw / ||| ||| H₂C H₂N 1 CH₂ | CH - n O H | H 0 H N H Q2Q
- Among these protein assays, which work in acidic conditions? a. Biuret assay b. Bicinchoninic acid assay c. Bradford assay d. Lowry assayFor this assignment I want you to look up some of the following compounds with their conjugate acid or base. Look up the compounds pka. Draw each compound in a solution that has a pH of 1, a pH of 7 and a pH of 11. Acetic acid Acetylsalicylic acid Triethylamine Alanine (this compound is amphoteric and has multiple acidic protons)The pka of the anilinium ion (conjugate acid of aminobenzene) is 4.6. At pH 1.0, it will exist mainly and occupy the water layer. At pH 4.6, as anilinium ion it will exist mainly as both aniline andailinium ion and occupy the both water and organic layer. At pH 14.0, it will exist mainly as aniline organic layer. and occupy the V
- Write general equations showing the ionization of a protein in acid medium and in basic medium. What medium favors acid ionization? Basic ionization?9. How do you know if a malenimide based reagent will conjugate to nitrogen or sulphur in an amino acid? но protein -protein SH NH2Draw a titration curve for the following peptide and circle the region(s) where this peptide would be a good buffer. Label the location on the titration curve where the peptide is least soluble: H-A-I-Y
- An electrophoresis experiment is performed with a sample containing the amino acid derivative shown. The pKa of the carboxylic acid group is 2.4, the pKa of the protonated amine group is 9.6, the pKa of the side chain as shown is 3.8. Describe where the amino acid derivative will migrate depending on the properties of the buffer used. Make a sound and complete argument to defend your response. HO H₂N OHFor the amino acid alanine, the major species in solution at pH 7 is the zwitterionic form, which has a negatively charged carboxylic acid group and a positively charged amino group. There is a less common neutral form in which neither group is charged. The carboxylic acid group of alanine has a p?apKa of 3.3. The amino group of alanine has a p?apKa of 8.8. Estimate the ratio of the concentration of the neutral amino acid species to the zwitterionic species at pH 7.1. Produce a reading outline for the chapter on amino acids and the section that introduces the peptide bond. Commit to memory the structures of the amino acids. 2. Draw a titration curve for the amino acid lysine using the pK s of 2.2, 9.0 and 10.0 for the ionizable groups of lysine. Use the titration curve in Model 1 and its description as a model for your drawing. Label the buffering regions and equivalence points. Draw the structures for the primary species of lysine at all the buffering regions and equivalence points you include in your graph. You might find it helpful to answer questions 1 and 2 to complete this. 3. Define the term buffering region and describe how you could locate the buffering region on a titration curve. 4. Define the term equivalence point and describe how you could locate the equivalence point on a titration curve. Model Titration Curve The graph below is a titration curve in which a solution of NaOH is added to a solution of propanoic acid (HPr). (This type…